Specific <scp>N</scp>‐terminal cleavage of ribosomal protein <scp>L</scp>27 in <scp><i>S</i></scp><i>taphylococcus aureus</i> and related bacteria

Wall, Erin A.; Caufield, J. Harry; Lyons, Charles E.; Manning, Keith A.; Dokland, Terje; Christie, Gail E.

doi:10.1111/mmi.12862

Cited by 25 publications

(53 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4E). It was recently reported that in S. aureus, bL27 has an extended N terminus that is cleaved posttranslationally after amino acid 9 by a specific essential protease, before or concurrent with ribosome assembly (44). In D50S, it reaches the acceptor stem of the P-site tRNA (40), whereas in T70S, it reaches the PTC and interacts with the CCA 3′ end of the P-site tRNA (6).…”

Section: Resultsmentioning

confidence: 99%

Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus

Eyal

Matzov

Krupkin

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

119

151

View full text Add to dashboard Cite

The emergence of bacterial multidrug resistance to antibiotics threatens to cause regression to the preantibiotic era. Here we present the crystal structure of the large ribosomal subunit from Staphylococcus aureus, a versatile Gram-positive aggressive pathogen, and its complexes with the known antibiotics linezolid and telithromycin, as well as with a new, highly potent pleuromutilin derivative, BC-3205. These crystal structures shed light on specific structural motifs of the S. aureus ribosome and the binding modes of the aforementioned antibiotics. Moreover, by analyzing the ribosome structure and comparing it with those of nonpathogenic bacterial models, we identified some unique internal and peripheral structural motifs that may be potential candidates for improving known antibiotics and for use in the design of selective antibiotic drugs against S. aureus.

show abstract

Section: Resultsmentioning

confidence: 99%

Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus

Eyal

Matzov

Krupkin

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

119

151

View full text Add to dashboard Cite

show abstract

“…Other families include peptidases that are effective during infection, by degrading antibodies (C66, M26 and M64); the generation of inhibitory peptides such as microcins (C96), and toxins (C10, C25, M30, N6, U69 and some peptidases from C60 and M4); or the degradation of antibiotics (M6, M56). Peptidases from other families are required for processing of proteins: C39 for bacteriocins, C108 for ribosomal protein L27 [36]; M90 for regulatory proteins.…”

Section: Familymentioning

confidence: 99%

Origins of peptidases

Rawlings

Bateman

2019

Biochimie

View full text Add to dashboard Cite

a b s t r a c tThe distribution of all peptidase homologues across all phyla of organisms was analysed to determine within which kingdom each of the 271 families originated. No family was found to be ubiquitous and even peptidases thought to be essential for life, such as signal peptidase and methionyl aminopeptides are missing from some clades. There are 33 peptidase families common to archaea, bacteria and eukaryotes and are assumed to have originated in the last universal common ancestor (LUCA). These include peptidases with different catalytic types, exo-and endopeptidases, peptidases with different tertiary structures and peptidases from different families but with similar structures. This implies that the different catalytic types and structures pre-date LUCA. Other families have had their origins in the ancestors of viruses, archaea, bacteria, fungi, plants and animals, and a number of families have had their origins in the ancestors of particular phyla. The evolution of peptidases is compared to recent hypotheses about the evolution of organisms.

show abstract

“…ERIC1_1c15570 was attributed to the cysteine protease Prp family. This family cleaves the N terminus extension of ribosomal subunit L27 in eubacteria (Wall et al 2015). ERIC1_1c21190 was attributed by InterPro to the type 2 phosphatidic acid phosphatases (PAP2) enzymes.…”

Section: Other Factorsmentioning

confidence: 99%

Unbiased random mutagenesis contributes to a better understanding of the virulent behaviour ofPaenibacillus larvae

et al. 2017

View full text Add to dashboard Cite

Aims: American foulbrood, caused by the Gram-positive bacteria Paenibacillus larvae, is one of the most severe bacterial diseases of the European honey bee. The bacterium has been known for long, but only the last decade the mechanisms used by the pathogen to cause disease in its host are starting to unravel. In this study, the knowledge of this virulent behaviour is expanded and several possible virulence factors are suggested. Methods and Results: Identification of possible virulence factors has been done by random mutagenesis to ensure an unbiased approach. A library of mutants was tested for a significant difference in virulence using in vitro exposure assays. Affected loci were characterized and their potential to contribute in virulence of the pathogen was assessed. Conclusions: The identified mutated loci dacB, dnaK, metN, ywqD, lysC, serC and gbpA are known to encode for virulence factors in other bacteria and are suggested to play a similar role in P. larvae. Significance and Impact of the Study: The study identified new possible virulence factors for P. larvae genotype ERIC I in an unbiased way. This contributes to the knowledge and understanding of the possible mechanisms used by this pathogen to colonize and kill its host.

show abstract

Specific N‐terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteria

Cited by 25 publications

References 43 publications

Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus

Structural insights into species-specific features of the ribosome from the pathogen Staphylococcus aureus

Origins of peptidases

Unbiased random mutagenesis contributes to a better understanding of the virulent behaviour ofPaenibacillus larvae

Contact Info

Product

Resources

About